TITLE:
Forward-Light-Scattering Characterization of Pre-Crystalline Aggregates in Crystallizing Lysozyme Solutions
AUTHORS:
Takashi Wakamatsu
KEYWORDS:
Protein Crystallization, Lysozyme, Light Scattering, Fractal Aggregation, Power Law
JOURNAL NAME:
American Journal of Analytical Chemistry,
Vol.5 No.9,
June
24,
2014
ABSTRACT: We present a method to characterize lysozyme pre-crystalline aggregates using a forward-light-scattering technique, which is highly sensitive to protein aggregates. The static light scattering properties at small angles of crystallizing lysozyme aggregates are discussed, and related to the crystallization conditions based on the concentration of added precipitant NaCl. Lysozyme solutions that started to crystallize because of precipitant exhibited profiles of forward light scattering that could be fitted by non-integer power laws, which indicated fractal aggregations of lysozyme had formed. Pre-crystalline solutions, in which lysozyme crystals later grew, had dense structural fractal clusters with fractal dimensions of D > 1.5. In contrast, solutions with aggregates in which crystals did not grow, had forward-light-scattering profiles that deviated from a power law or had lower power values.